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plsX plsX plsY plsY plsB plsB fabD fabD rpmF rpmF fabH2 fabH2 rpsM rpsM rplO rplO fabI fabI rpsH rpsH rplR rplR
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
plsXFatty acid biosynthesis protein PlsX; Catalyzes the reversible formation of acyl-phosphate (acyl- PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. (326 aa)    
Predicted Functional Partners:
plsY
Conserved hypothetical protein; Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
 
  
 0.998
plsB
Glycerol-3-phosphate acyltransferase; Product name confidence: Class 2 (High similarity to functionally studied protein); Belongs to the GPAT/DAPAT family.
   
 
 0.991
fabD
malonyl-CoA-[acyl-carrier-protein] transacylase; Product name confidence: Class 1 (Function experimentally demonstrated in P. aeruginosa).
 
  
 0.972
rpmF
50S ribosomal protein L32; Product name confidence: Class 2 (High similarity to functionally studied protein); Belongs to the bacterial ribosomal protein bL32 family.
  
  
 0.963
fabH2
3-oxoacyl-[acyl-carrier-protein] synthase III; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids; Belongs to the thiolase-like superfamily. FabH family.
  
  
 0.919
rpsM
30S ribosomal protein S13; Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. Belongs to the universal ribosomal protein uS13 family.
   
    0.892
rplO
50S ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
  
    0.876
fabI
NADH-dependent enoyl-ACP reductase; Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity); Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.
   
  
 0.872
rpsH
30S ribosomal protein S8; One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit; Belongs to the universal ribosomal protein uS8 family.
   
    0.869
rplR
50S ribosomal protein L18; This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
   
    0.851
Your Current Organism:
Pseudomonas aeruginosa
NCBI taxonomy Id: 208964
Other names: P. aeruginosa PAO1, Pseudomonas aeruginosa PAO1, Pseudomonas sp. PAO1
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